Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
Y171F/P173L/N174K | mutation results in 20000fold decrease in the reaction rate and reduced binding affinity | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000093 | - |
12-mer oligodeoxyribonucleotide containing a natural AP site | wild-type, pH 7.5, 25°C | Homo sapiens | |
0.000098 | - |
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site | wild-type, pH 7.5, 25°C | Homo sapiens | |
0.00022 | - |
12-mer oligodeoxyribonucleotide containing a natural AP site | mutant Y171F/P173L/N174K, pH 7.5, 25°C | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
12-mer oligodeoxyribonucleotide containing a 2'-deoxyguanosine at the natural AP site | - |
Homo sapiens | ? | - |
? | |
12-mer oligodeoxyribonucleotide containing a natural AP site | the minimal kinetic model for the natural AP site incision consists of four stages corresponding to three different transient states of APE1. When the enzyme is complexed with the AP-substrate, the catalytic cycle is completed within 3 s | Homo sapiens | ? | - |
? | |
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site | - |
Homo sapiens | ? | - |
? | |
additional information | wild-type APE1 undergoes at least four conformational transitions during the processing of abasic sites in DNA. Nonspecific interactions of APE1 with undamaged DNA can be described by a two-step kinetic scheme. APE1 molecule undergoes at least four conformational transitions, including nonspecific encounter complex formation, mutual adjustment of the enzyme and DNA substrate structures for catalysis, catalytic incision of the substrate, and release of the enzyme from its complex with the product. The C1'-hydroxyl moiety of the abasic site is required for the most effective recognition and catalysis | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AP endonuclease 1 | - |
Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000153 | - |
12-mer oligodeoxyribonucleotide containing a natural AP site | mutant Y171F/P173L/N174K, pH 7.5, 25°C | Homo sapiens | |
1 | - |
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site | wild-type, pH 7.5, 25°C | Homo sapiens | |
2.8 | - |
12-mer oligodeoxyribonucleotide containing a natural AP site | wild-type, pH 7.5, 25°C | Homo sapiens |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.63 | - |
12-mer oligodeoxyribonucleotide containing a natural AP site | mutant Y171F/P173L/N174K, pH 7.5, 25°C | Homo sapiens | |
10000 | - |
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site | wild-type, pH 7.5, 25°C | Homo sapiens | |
30000 | - |
12-mer oligodeoxyribonucleotide containing a natural AP site | wild-type, pH 7.5, 25°C | Homo sapiens |